Abstract
Taurine (2-aminoethanesulfonic acid) is primarily transported by its carrier, the taurine transporter, the gene for which has been cloned recently from several species and tissues 1–5. Expression of the taurine transporter gene (TauT) is regulated by many factors, including the p53 tumor suppressor gene, Wilms’ tumor suppressor gene (WT1), Sp1 transcription factor, and dietary taurine manipulation 6–9. In contrast, the taurine transporter itself, which contains 12 hydrophobic membrane-spanning domains, is mainly regulated by protein kinase C (PKC) phosphorylation 10. Our previous studies show that the fourth intracellular segment (S4) of the taurine transporter may be involved in the gating of taurine transport that is modulated by PKC phosphorylation of Ser-322 located in S4 11. In the present study, the role of charged amino acid residues located in S4 in the gating of taurine transport was determined using site-directed mutagenesis and the Xenopus laevis oocyte expression system.
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References
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Han, X., Patters, A.B., Chesney, R.W. (2003). Gating of Taurine Transport. In: Lombardini, J.B., Schaffer, S.W., Azuma, J. (eds) Taurine 5. Advances in Experimental Medicine and Biology, vol 526. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0077-3_19
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DOI: https://doi.org/10.1007/978-1-4615-0077-3_19
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